Direct interaction of Ca2+/calmodulin inhibits histone deacetylase 5 repressor core binding to myocyte enhancer factor 2.
Myocyte enhancer factor 2 (MEF2) proteins play a pivotal role in the differentiation of cardiac and skeletal muscle cells. MEF2 factors are regulated by histone deacetylase enzymes such as histone deacetylase 5 (HDAC5). HDAC5 in turn is responsive to Ca(2+) signaling mediated by the intracellular calcium sensor calmodulin. Here a ... combination of proteolytic fragmentation, matrix-assisted laser desorption ionization mass spectrometry, Edman degradation, circular dichroism, gel filtration, and surface plasmon resonance studies is utilized to define and characterize a stable core domain of HDAC5 and to examine its interactions with MEF2a and calmodulin. Results from real time binding experiments provide evidence for direct interaction of Ca(2+)/calmodulin with HDAC5 inhibiting MEF2a association with this enzyme.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Calcium, Calmodulin, Cells, Cultured, Chromatography, Gel, Circular Dichroism, DNA-Binding Proteins, Egtazic Acid, Histone Deacetylase Inhibitors, Histone Deacetylases, Humans, Kinetics, MADS Domain Proteins, Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Mutation, Myogenic Regulatory Factors, Promoter Regions, Genetic, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Surface Plasmon Resonance, Time Factors, Transcription Factors, Trypsin
Amino Acid Motifs, Amino Acid Sequence, Calcium, Calmodulin, Cells, Cultured, Chromatography, Gel, Circular Dichroism, DNA-Binding Proteins, Egtazic Acid, Histone Deacetylase Inhibitors, Histone Deacetylases, Humans, Kinetics, MADS Domain Proteins, Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Mutation, Myogenic Regulatory Factors, Promoter Regions, Genetic, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Surface Plasmon Resonance, Time Factors, Transcription Factors, Trypsin
J. Biol. Chem.
Date: May. 16, 2003
PubMed ID: 12626519
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